MolNFT v1 · #166766 · protein
Crystal structure of beta-2 glycoprotein I purified from plasma (PB2GPI)
6V06 · Beta-2-glycoprotein 1: “Crystal structure of beta-2 glycoprotein I purified from plasma (PB2GPI)”. X-ray diffraction, 4 ligands (NAG, MAN, BMA), 1 pocket (best druggability 0.51). MolNFT v1 #166766 on GenesisL1: 3D structure…
- PDB
- 6V06
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-2-glycoprotein 1
- UniProt
- P02749
- Ligands
- NAG, MAN, BMA, SO4
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-2-glycoprotein 1 | protein | 326 | 2% helix, 41% strand | P02749 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 13 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 7 copies
- BMA · beta-D-mannopyranose · sugar · 6 copies
- SO4 · Sulfate ion · ion · 13 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.51 | 0.83 | 24 | SO4 |
Modifications
Observed in the structure: 11 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 6V06 · Crystal structure of Beta-2 glycoprotein I purified from plasma (pB2GPI) · the same entry in another collection · chain A against A, TM-score 1.00
- P02749 · AlphaFold monomer V2.0 prediction for beta-2-glycoprotein 1 (P02749) · a predicted model of the same protein · chain A against A, TM-score 0.89
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P02749
- Elsewhere: RCSB PDB 6V06 · PDBe 6V06 · UniProt P02749
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